LAD1_MOUSE
ID LAD1_MOUSE Reviewed; 528 AA.
AC P57016;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Ladinin-1;
DE Short=Lad-1;
DE AltName: Full=Linear IgA disease antigen homolog;
DE Short=LADA;
GN Name=Lad1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=9119369; DOI=10.1006/geno.1996.4507;
RA Motoki K., Megahed M., LaForgia S., Uitto J.;
RT "Cloning and chromosomal mapping of mouse ladinin, a novel basement
RT membrane zone component.";
RL Genomics 39:323-330(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-56; SER-62; SER-72;
RP SER-76; SER-328; SER-358 AND SER-367, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Anchoring filament protein which is a component of the
CC basement membrane zone. {ECO:0000269|PubMed:9119369}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000269|PubMed:9119369}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, lung and keratinocytes
CC followed by liver, spleen and brain. Not expressed in testis, skeletal
CC and heart muscle and in fibroblasts. {ECO:0000269|PubMed:9119369}.
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DR EMBL; U58011; AAC53044.1; -; mRNA.
DR EMBL; AK083526; BAC38941.1; -; mRNA.
DR EMBL; BC016257; AAH16257.1; -; mRNA.
DR EMBL; BC031131; AAH31131.1; -; mRNA.
DR CCDS; CCDS35723.1; -.
DR RefSeq; NP_598425.2; NM_133664.3.
DR AlphaFoldDB; P57016; -.
DR BioGRID; 201090; 2.
DR STRING; 10090.ENSMUSP00000044630; -.
DR iPTMnet; P57016; -.
DR PhosphoSitePlus; P57016; -.
DR EPD; P57016; -.
DR jPOST; P57016; -.
DR MaxQB; P57016; -.
DR PaxDb; P57016; -.
DR PeptideAtlas; P57016; -.
DR PRIDE; P57016; -.
DR ProteomicsDB; 264906; -.
DR Antibodypedia; 20642; 159 antibodies from 25 providers.
DR Ensembl; ENSMUST00000038760; ENSMUSP00000044630; ENSMUSG00000041782.
DR GeneID; 16763; -.
DR KEGG; mmu:16763; -.
DR UCSC; uc007ctt.1; mouse.
DR CTD; 3898; -.
DR MGI; MGI:109343; Lad1.
DR VEuPathDB; HostDB:ENSMUSG00000041782; -.
DR eggNOG; ENOG502S2ZW; Eukaryota.
DR GeneTree; ENSGT00390000005256; -.
DR HOGENOM; CLU_038228_0_0_1; -.
DR InParanoid; P57016; -.
DR OMA; LWISKTQ; -.
DR OrthoDB; 976869at2759; -.
DR PhylomeDB; P57016; -.
DR TreeFam; TF335896; -.
DR BioGRID-ORCS; 16763; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Lad1; mouse.
DR PRO; PR:P57016; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P57016; protein.
DR Bgee; ENSMUSG00000041782; Expressed in esophagus and 137 other tissues.
DR Genevisible; P57016; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR InterPro; IPR017404; Ladinin_1.
DR PANTHER; PTHR12392; PTHR12392; 1.
DR PIRSF; PIRSF038144; Ladinin_1; 1.
PE 1: Evidence at protein level;
KW Basement membrane; Extracellular matrix; Phosphoprotein;
KW Reference proteome; Repeat; Secreted.
FT CHAIN 1..528
FT /note="Ladinin-1"
FT /id="PRO_0000084350"
FT REPEAT 184..186
FT /note="SEK 1"
FT REPEAT 190..192
FT /note="SEK 2"
FT REPEAT 202..204
FT /note="SEK 3"
FT REPEAT 208..210
FT /note="SEK 4"
FT REPEAT 269..271
FT /note="SEK 5"
FT REPEAT 279..281
FT /note="SEK 6"
FT REGION 1..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..281
FT /note="6 X SEK repeats"
FT REGION 492..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00515"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00515"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00515"
SQ SEQUENCE 528 AA; 58864 MW; 3893C72B0C92609C CRC64;
MSVSRKDWSA LSSLARQRTL EDEEEQERER RRRHRNLSST TDDESPKLTQ NGAQRSVERL
PSVEEAEVSK PSPPASKDED EDFQAILRTR KERRQRRQVV EAVQAPVQER PEAEEERDSL
GPEQTSSQPL VPKKKVEALP RRRLSREQRG PWAQDEERLK NRELAEGEKR LPEETVAQQK
TLVSEKTPVS EKTPVPAKRL VSEKACPSEK GTATEKASLT EKRHSPEKLV PEKTSVTEKS
PVPEKTLVSL KTAAPERRSP PVLEKAIVSE KMQERKLVSE KASIFEKSLV SEAKLTPKKA
AVSEQPQTTG GSQATTREPR GRALPDKSPP SSAEQSTPAP PTKASRFPPI TLQVKIPSKD
EDADTPSPTL LTYSSSLKRS SPRTISFRMS PRKDNSETPL TRSASVRLPA STVKLGEKLE
RYHTAIQRSE SVRSPGSSRT EVLVTPAGVA SKRHLFEKEL SGQNRTEPTS IRKENLRLSG
VVTSRLNLWI SKTQDSGDHG SQEVRKEASV TKRAQWGSKP STSLDAEV
